Cargando…
Characterisation of the Structure and Oligomerisation of Islet Amyloid Polypeptides (IAPP): A Review of Molecular Dynamics Simulation Studies
Human islet amyloid polypeptide (hIAPP) is a naturally occurring, intrinsically disordered protein whose abnormal aggregation into amyloid fibrils is a pathological feature in type 2 diabetes, and its cross-aggregation with amyloid beta has been linked to an increased risk of Alzheimer’s disease. Th...
Autores principales: | Moore, Sandra J., Sonar, Krushna, Bharadwaj, Prashant, Deplazes, Evelyne, Mancera, Ricardo L. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6225196/ https://www.ncbi.nlm.nih.gov/pubmed/30149632 http://dx.doi.org/10.3390/molecules23092142 |
Ejemplares similares
-
Influence of force field choice on the conformational landscape of rat and human islet amyloid polypeptide
por: Moore, Sandra J., et al.
Publicado: (2022) -
Myricetin Inhibits Islet Amyloid Polypeptide (IAPP) Aggregation and Rescues Living Mammalian Cells from IAPP Toxicity
por: Zelus, Casey, et al.
Publicado: (2012) -
Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization
por: Mishra, Aseem, et al.
Publicado: (2013) -
β-Hairpin Peptide Mimics Decrease Human Islet Amyloid Polypeptide (hIAPP) Aggregation
por: Lesma, Jacopo, et al.
Publicado: (2021) -
Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice
por: Franko, Andras, et al.
Publicado: (2018)